2bty

From Proteopedia

Revision as of 12:19, 30 October 2007

ACETYLGLUTAMATE KINASE FROM THERMOTOGA MARITIMA COMPLEXED WITH ITS INHIBITOR ARGININE

Overview

N-Acetylglutamate kinase (NAGK) catalyses the second step in the route of, arginine biosynthesis. In many organisms this enzyme is inhibited by the, final product of the route, arginine, and thus plays a central regulatory, role. In addition, in photosynthetic organisms NAGK is the target of the, nitrogen-signalling protein PII. The 3-D structure of homodimeric, arginine-insensitive, Escherichia coli NAGK, clarified substrate binding, and catalysis but shed no light on arginine inhibition of NAGK. We now, shed light on arginine inhibition by determining the crystal structures, at 2.75 A and 2.95 A resolution, of arginine-complexed Thermotoga maritima, and arginine-free Pseudomonas aeruginosa NAGKs, respectively. Both enzymes, are highly similar ring-like hexamers having a central orifice ... [(full description)]

About this Structure

2BTY is a [Single protein] structure of sequence from [Thermotoga maritima] with K, ARG and NLG as [ligands]. This structure superseeds the now removed PDB entry 1UVV. Active as [Acetylglutamate kinase], with EC number [2.7.2.8]. Structure known Active Site: ARG. Full crystallographic information is available from [OCA].

Reference

Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa., Ramon-Maiques S, Fernandez-Murga ML, Gil-Ortiz F, Vagin A, Fita I, Rubio V, J Mol Biol. 2006 Feb 24;356(3):695-713. Epub 2005 Dec 12. PMID:16376937

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